Division of Redox Regulation

PD Dr. Tobias P. Dick

A genetically encoded biosensor for the glutathione redox potential shows intratumoral redox heterogeneity on a tissue section.
© dkfz.de

For a long time, reactive oxygen species have been mostly regarded as unwanted and damaging side-products of cellular metabolism. However, it has become clear that some of these species, in particular hydrogen peroxide (H2O2), play important positive roles as signaling molecules, and thus are essential for organismal health. Oxidative signals are now recognized to trigger adaptive responses and adequate cell fate decisions. The signaling function of H2O2 is based on the reversible oxidative modification of transcription factors and other proteins involved in cell regulation. Our special attention is devoted to the molecular mechanisms by which H2O2 achieves specificity as a signaling molecule. We are investigating signaling pathways by which endogenous H2O2 contributes to metabolic stress adaptation and cytoprotection. Furthermore, we aim to understand how tumor cells take advantage of redox signaling pathways.

We will continue to investigate the molecular mechanisms of redox signaling, in particular the role of peroxidases as primary oxidant receptors and mediators of regulatory protein oxidation. We will continue to make use of mechanistic insights to create tools that enable the visualization and manipulation of defined redox signals inside living cells and model organisms. We will employ these tools to obtain understanding of redox homeostasis in healthy and malignant situations. In particular, we are interested in intervention strategies that enhance cytoprotective redox signals in healthy cells and prevent them in malignant cells.


PD Dr. Tobias P. Dick
Redox Regulation (A160)
Deutsches Krebsforschungszentrum
Im Neuenheimer Feld 280
69120 Heidelberg
Tel: +49 6221 42 2320

Selected Publications

  • Peralta, D. et al. (2015). A proton relay enhances H2O2 sensitivity of GAPDH to facilitate metabolic adaptation. Nat Chem Biol, 11(2), 156-163.
  • Sobotta, M.C. et al. (2015). Peroxiredoxin-2 and STAT3 form a redox relay for H2O2 signaling. Nat Chem Biol, 11(1), 64-70.
  • Morgan, B. et al. (2013). Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat Chem Biol, 9(2), 119–125.
  • Albrecht, S.C. et al. (2011). In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis. Cell Metab, 14(6), 819–829.
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